issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

May 2008 issue

Highlighted illustration

Cover illustration: Neutron Laue diffraction pattern recorded from a hydrogenated thaumatin crystal using the LADI-III instrument at the ILL (pictured bottom left) (Teixeira, Blakeley, Leal, Mitchell & Forsyth, p. 378).

protein structure communications


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Structures of BA0252, an alanine racemase from B. anthracis, in the presence and absence of the inhibitor (R)-1-aminoethylphosphonic acid (L-Ala-P) and determined by X-ray crystallography to resolutions of 2.1 and 1.47 Å, respectively, are described.

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The crystal structure of the plasmid-mediated class C β-lactamase ACT-1 has been solved at 2.4 Å resolution.

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The crystal structure of an acetyltransferase encoded by the gene PA1377 from Pseudomonas aeruginosa has been determined at 2.25 Å resolution. Comparison with a related acetyltransferase revealed a structural difference in the active site that was taken to reflect a difference in substrate binding and/or specificity between the two enzymes.

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The crystal structure of S. aureus 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase has been determined at 1.7 Å resolution in complex with formycin A.

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The X-ray structure of human CutA1 was solved in space group P212121, with unit-cell parameters a = 68.69, b = 88.84, c = 125.33 Å and six molecules per asymmetric unit.

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The crystal structure of 3-oxoacyl-(acyl-carrier protein) synthase II from T. thermophilus HB8 has been determined at 2.0 Å resolution and compared with the structures of β-keto-ACP synthases from other sources.

crystallization communications


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Rv2780, an alanine dehydrogenase from M. tuberculosis, has been crystallized in apo and NAD/pyruvate-bound forms. Preliminary crystallographic analysis shows that there is a hexamer and trimer in the asymmetric units of the apo and ternary complex forms, respectively.

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A chitinase isolated from the latex of the tropical species Carica papaya has been crystallized. The addition of N-acetyl-D-glucosamine to the crystallization solution has improved the diffraction quality resolution of the crystal to 1.8 Å resolution.

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The flavodoxin NifF from R. capsulatus, a candidate for nitrogenase reduction during nitrogen fixation, has been crystallized using the hanging-drop vapour-diffusion method. Preliminary X-ray data processing at 2.17 Å resolution allowed determination of the crystal system and unit-cell parameters.

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Preliminary neutron crystallographic data from the sweet protein thaumatin have been recorded using the LADI-III diffractometer at the Institut Laue Langevin (ILL). The results illustrate the feasibility of a full neutron structural analysis aimed at further understanding the molecular basis of the perception of sweet taste. Such an analysis will exploit the use of perdeuterated thaumatin.

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Crystals of the phosphotyrosine-binding domain 1 (PTB1) of the neuronal adaptor protein Fe65 grown in the presence of a mercury derivative show a dramatic improvement in resolution, permitting SAD phasing.

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The haem-binding protein HbpS from Streptomyces reticuli was crystallized and diffraction data were collected to a maximal resolution of 2.25 Å.

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A periplasmic membrane-fusion protein MacA from Actinobacillus actinomycetemcomitans, an essential component of the multidrug efflux pump in Gram-negative bacteria, was crystallized.

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Decameric and monomeric forms of recombinant C49S mutant AhpC from H. pylori have been crystallized. Diffraction data were collected to 2.8 and 2.25 Å, respectively.

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The cloning, purification and crystallization of a bacterioferritin from M. tuberculosis together with preliminary X-ray characterization of its crystals are reported.

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C. reinhardtii centrin, an EF-hand calcium-binding protein localized to the microtubule-organizing center of eukaryotic organisms, has been crystallized in the presence of the model peptide melittin. X-ray diffraction data were collected to 2.2 Å resolution.

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The Hyp-1 protein suggested to be a phenolic oxidative-coupling enzyme involved in the biosynthesis of hypericin, a medicinally important natural compound found in St John's wort (H. perforatum), has been expressed, purified and prepared in single-crystal form.

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Alzheimer's disease is characterized by proteolytic processing of the amyloid precursor protein (APP), which releases the aggregation-prone amyloid-β (Aβ) peptide and liberates the intracellular domain (AICD) that interacts with various adaptor proteins. The crystallized AICD–Fe65-PTB2 complex is of central importance for APP translocation, nuclear signalling, processing and Aβ generation.

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The crystallization strategy for the RNA polymerase I subcomplex A14/A43, which is based on iterative cycles of prediction, probing and removal of four flexible protein regions, is described.

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The catalytic domain of collagenase G from C. histolyticum was expressed in E. coli BL21 (DE3) and purified using affinity and size-exclusion column-chromatographic methods. Crystals were obtained at 290 K by the sitting-drop vapour-diffusion method and diffraction data have been collected to 2.75 Å resolution.

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Preliminary X-ray diffraction studies of a novel ring-cleaving enzyme from B. xenovorans LB400 encoded by the benzoate-oxidation (box) pathway.

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Preliminary X-ray diffraction studies of the bradyzoite-specific surface antigen BSR4 from T. gondii are described.

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MAP2569c from M. avium subsp. paratuberculosis, a putative glycosyltransferase implicated in mycobacterial cell-wall biosynthesis, was cloned, expressed, purified and crystallized. X-ray diffraction data were collected to 1.8 Å resolution.

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The double mutant D30P/A31G of the Rop protein was crystallized with the aim of analyzing the loop region as a possible folding-control element. The crystals belonged to space group P21 and diffracted to 1.4 Å resolution.

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Good-quality crystals of selenomethionine-substituted Msmeg_3380 were obtained by the hanging-drop vapour-diffusion technique and diffracted to 1.2 Å using synchrotron radiation.

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Crystallization and X-ray diffraction data collection of the Fab fragment of the monoclonal antibody WO2 in the absence or presence of amyloid β peptides associated with Alzheimer's disease are reported.
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